› 1o5l

X-ray diffraction
2.3Å resolution

Crystal structure of Transcriptional regulator (TM1171) from Thermotoga maritima at 2.30 A resolution

Released:
DOI: 10.2210/pdb1o5l/pdb
PDB entry 1o5l coloured by chain, front view.
PDB entry 1o5l coloured by chain, side view.
PDB entry 1o5l coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.
Spraggon G, Pantazatos D, Klock HE, Wilson IA, Woods VL, Lesley SA
Protein Sci 13 3187-99 (2004)
PMID: 15557262

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194735 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional regulator, crp family Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 24.9 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0Q3 (Residues: 1-201; Coverage: 100%)
Gene name: TM_1171
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P6122
Unit cell:
a: 62.971Å b: 62.971Å c: 167.103Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.253
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
3 more

1 mention without citation

On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.
Spraggon et al. (2004)